Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Gag-pro-pol[Gene ID: 1491941 ]
♦Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA)
♦ Capsid protein p24 (CA)
♦ Nucleocapsid protein p15-pro (NC') (NC-pro)
♦ Protease (PR) (EC 3.4.23.-)
♦ p1
♦ Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
♦ Capsid protein p24 (CA)
♦ Nucleocapsid protein p15-pro (NC') (NC-pro)
♦ Protease (PR) (EC 3.4.23.-)
♦ p1
♦ Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
Human T-cell Leukemia Virus 2 (HTLV-2)
Viruses> Retro-transcribing Viruses> Retroviridae> Orthoretrovirinae> Deltaretrovirus> Primate T-lymphotropic Virus 2> Human T-cell Leukemia Virus 2 (HTLV-2)
Not Available
Various pathway(s) in which protein is involved
Not Available
MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAP
VPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCS
SLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTP
KEPILRSLAYSNANKECQKILQARGHTNSPLGEMLRTCQAWTPKDKTKVLVVQPRRPPPTQPCFRCGKVGHWSRDCTQPRPPPGPCPLCQDPSHWKRDCP
QLKPPQEEGEPLLLDLPSTSGTTEEKNLLKGGDLISPHPDQDISILPLIPLRQQQQPILGVRISVMGQTPQPTQALLDTGADLTVIPQTLVPGPVKLHDT
LILGASGQTNTQFKLLQTPLHIFLPFRRSPVILSSCLLDTHNKWTIIGRDALQQCQGLLYLPDDPSPHQLLPIATPNTIGLEHLPPPPQVDQFPLNLPER
LQALNDLVSKALEAGHIEPYSGPGNNPVFPVKKPNGKWRFIHDLRATNAITTTLTSPSPGPPDLTSLPTALPHLQTIDLTDAFFQIPLPKQYQPYFAFTI
PQPCNYGPGTRYAWTVLPQGFKNSPTLFEQQLAAVLNPMRKMFPTSTIVQYMDDILLASPTNEELQQLSQLTLQALTTHGLPISQEKTQQTPGQIRFLGQ
VISPNHITYESTPTIPIKSQWTLTELQVILGEIQWVSKGTPILRKHLQSLYSALHGYRDPRACITLTPQQLHALHAIQQALQHNCRGRLNPALPLLGLIS
LSTSGTTSVIFQPKQNWPLAWLHTPHPPTSLCPWGHLLACTILTLDKYTLQHYGQLCQSFHHNMSKQALCDFLRNSPHPSVGILIHHMGRFHNLGSQPSG
PWKTLLHLPTLLQEPRLLRPIFTLSPVVLDTAPCLFSDGSPQKAAYVLWDQTILQQDITPLPSHETHSAQKGELLALICGLRAAKPWPSLNIFLDSKYLI
KYLHSLAIGAFLGTSAHQTLQAALPPLLQGKTIYLHHVRSHTNLPDPISTFNEYTDSLILAPLVPLTPQGLHGLTHCNQRALVSFGATPREAKSLVQTCH
TCQTINSQHHMPRGYIRRGLLPNHIWQGDVTHYKYKKYKYCLHVWVDTFSGAVSVSCKKKETSCETISAVLQAISLLGKPLHINTDNGPAFLSQEFQEFC
TSYRIKHSTHIPYNPTSSGLVERTNGVIKNLLNKYLLDCPNLPLDNAIHKALWTLNQLNVMNPSGKTRWQIHHSPPLPPIPEASTPPKPPPKWFYYKLPG
LTNQRWKGPLQSLQEAAGAALLSIDGSPRWIPWRFLKKAACPRPDASELAEHAATDHQHHG
VPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCS
SLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTP
KEPILRSLAYSNANKECQKILQARGHTNSPLGEMLRTCQAWTPKDKTKVLVVQPRRPPPTQPCFRCGKVGHWSRDCTQPRPPPGPCPLCQDPSHWKRDCP
QLKPPQEEGEPLLLDLPSTSGTTEEKNLLKGGDLISPHPDQDISILPLIPLRQQQQPILGVRISVMGQTPQPTQALLDTGADLTVIPQTLVPGPVKLHDT
LILGASGQTNTQFKLLQTPLHIFLPFRRSPVILSSCLLDTHNKWTIIGRDALQQCQGLLYLPDDPSPHQLLPIATPNTIGLEHLPPPPQVDQFPLNLPER
LQALNDLVSKALEAGHIEPYSGPGNNPVFPVKKPNGKWRFIHDLRATNAITTTLTSPSPGPPDLTSLPTALPHLQTIDLTDAFFQIPLPKQYQPYFAFTI
PQPCNYGPGTRYAWTVLPQGFKNSPTLFEQQLAAVLNPMRKMFPTSTIVQYMDDILLASPTNEELQQLSQLTLQALTTHGLPISQEKTQQTPGQIRFLGQ
VISPNHITYESTPTIPIKSQWTLTELQVILGEIQWVSKGTPILRKHLQSLYSALHGYRDPRACITLTPQQLHALHAIQQALQHNCRGRLNPALPLLGLIS
LSTSGTTSVIFQPKQNWPLAWLHTPHPPTSLCPWGHLLACTILTLDKYTLQHYGQLCQSFHHNMSKQALCDFLRNSPHPSVGILIHHMGRFHNLGSQPSG
PWKTLLHLPTLLQEPRLLRPIFTLSPVVLDTAPCLFSDGSPQKAAYVLWDQTILQQDITPLPSHETHSAQKGELLALICGLRAAKPWPSLNIFLDSKYLI
KYLHSLAIGAFLGTSAHQTLQAALPPLLQGKTIYLHHVRSHTNLPDPISTFNEYTDSLILAPLVPLTPQGLHGLTHCNQRALVSFGATPREAKSLVQTCH
TCQTINSQHHMPRGYIRRGLLPNHIWQGDVTHYKYKKYKYCLHVWVDTFSGAVSVSCKKKETSCETISAVLQAISLLGKPLHINTDNGPAFLSQEFQEFC
TSYRIKHSTHIPYNPTSSGLVERTNGVIKNLLNKYLLDCPNLPLDNAIHKALWTLNQLNVMNPSGKTRWQIHHSPPLPPIPEASTPPKPPPKWFYYKLPG
LTNQRWKGPLQSLQEAAGAALLSIDGSPRWIPWRFLKKAACPRPDASELAEHAATDHQHHG
1461
Not Available
Not Available
23-01-2007
Evidence at protein level
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
♦Gag-Pro-Pol polyprotein: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.
♦ Matrix protein p19: Matrix protein.
♦ Capsid protein p24: Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.
♦ Nucleocapsid protein p15-pro: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.
♦ Protease: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (By similarity).
♦ Reverse transcriptase/ribonuclease H: RT is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'-endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Pro binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).
♦ Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions.
♦ Matrix protein p19: Matrix protein.
♦ Capsid protein p24: Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.
♦ Nucleocapsid protein p15-pro: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.
♦ Protease: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (By similarity).
♦ Reverse transcriptase/ribonuclease H: RT is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'-endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Pro binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).
♦ Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions.
3.4.23.- , 2.7.7.49 , 2.7.7.7 , 3.1.26.4 , 2.7.7.- , 3.1.-.-
GO:0003677 ; GO:0003887 ; GO:0003964 ; GO:0004190 ; GO:0004523 ;
GO:0005198 ; GO:0006310 ; GO:0008270 ; GO:0015074 ; GO:0019013 ;
GO:0039657 ; GO:0044826 ; GO:0046718 ; GO:0075713
GO:0005198 ; GO:0006310 ; GO:0008270 ; GO:0015074 ; GO:0019013 ;
GO:0039657 ; GO:0044826 ; GO:0046718 ; GO:0075713
♦ Matrix protein p19: Virion .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p15-pro: Virion .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p15-pro: Virion .
♦DOMAIN 473 551 Peptidase A2.
♦ DOMAIN 612 802 Reverse transcriptase.
♦ DOMAIN 1029 1164 RNase H.
♦ DOMAIN 1218 1387 Integrase catalytic.
♦ DOMAIN 612 802 Reverse transcriptase.
♦ DOMAIN 1029 1164 RNase H.
♦ DOMAIN 1218 1387 Integrase catalytic.
MOTIF 94 97 PTAP/PSAP motif.; MOTIF 124 127 PPXY motif. ; MOTIF 130 133 PTAP/PSAP motif.
NMR spectroscopy (1)
♦ACT_SITE 478 478 For protease activity
♦ shared with dimeric partner.
♦ shared with dimeric partner.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
- Million Molecules
Best 20 Hit molecules
Not Available